Multiple protein kinases affect the responses of dorsal horn neurons through phosphorylation of synaptic receptors\r\nand proteins involved in intracellular signal transduction pathways, and the consequences of this modulation may\r\nbe spinal central sensitization. In contrast, the phosphatases catalyze an opposing reaction of de-phosphorylation,\r\nwhich may also modulate the functions of crucial proteins in signaling nociception. This is an important\r\nmechanism in the regulation of intracellular signal transduction pathways in nociceptive neurons. Accumulated\r\nevidence has shown that phosphatase 2A (PP2A), a serine/threonine specific phosphatase, is implicated in synaptic\r\nplasticity of the central nervous system and central sensitization of nociception. Therefore, targeting protein\r\nphosphotase 2A may provide an effective and novel strategy for the treatment of clinical pain. This review will\r\ncharacterize the structure and functional regulation of neuronal PP2A and bring together recent advances on the\r\nmodulation of PP2A in targeted downstream substrates and relevant multiple nociceptive signaling molecules
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